The rationale for a carbon ion radiation therapy facility in Australia.

Australia has taken a collaborative nationally networked approach to achieve particle therapy capability. This supports the under-construction proton therapy facility in Adelaide, other potential proton centres and an under-evaluation proposal for a hybrid carbon ion and proton centre in western Sydney. A wide-ranging overview is presented of the rationale for carbon ion radiation therapy, applying observations to the case for an Australian facility and to the clinical and research potential from such a national centre.

First experiments on the Australian Synchrotron Imaging and Medical beamline, including investigations of the effective source size in respect of X-ray imaging.

The Imaging and Medical beamline at the Australian Synchrotron achieved ;first light' in December 2008. Here, the first experiments performed on the beamline are reported, which involved both X-ray imaging and tomography studies for a range of samples. The use of a plastic-edge phantom for quantitative measurements of contrast and resolution proved to be very instructive and helped to confirm certain parameter values such as the effective horizontal source size, detector resolution and average X-ray energy for the polychromatic beam.

Time-resolved grazing-incidence diffraction studies of thin films using an imaging-plate camera and focusing monochromator.

A multiple imaging-plate (IP) detector system and focusing monochromator have been developed and successfully applied to the time-resolved study of phase transitions in Langmuir-Blodgett (LB) films by grazing-incidence X-ray diffraction (GIXD). The first reported application of imaging plates to a GIXD study was carried out by our group and proved to be very successful in the determination of thin-film structure [Foran, Peng, Steitz, Barnes & Gentle (1996). Langmuir, 12, 774-777].

Multiple-wavelength powder diffraction using imaging plates at the Australian National Beamline.

The Australian powder diffractometer at the Photon Factory is capable of recording multiple powder-diffraction scans in less than 5 min per pattern using imaging plates in Debye-Scherrer geometry. This, coupled with incrementing the X-ray beam energy in suitably small steps (down to approximately 2 eV) between exposures, allows fast collection of anomalous diffraction data. Data collected from a copper oxide-based superconductor at energies near the Cu K-absorption edge are presented, along with an account of the technique used to extract multiple-exposure powder-diffraction data from imaging plates.

An eight-position capillary sample spinning stage for the diffractometer at BL20B at the Photon Factory.

An eight-position capillary sample spinning stage has been developed for use in conjunction with the versatile vacuum diffractometer (BIGDIFF) at BL20B at the Photon Factory. BIGDIFF is often used in its powder diffraction mode using powders mounted in capillaries and up to eight imaging plates to record the diffraction pattern from the sample. Using the multiple spinning stage a number of diffraction patterns can be recorded on the imaging plates if the imaging-plate cassette is moved behind the Weissenberg screen to a new position after exposure of the sample to the beam.

Focusing monochromator and imaging-plate camera for grazing-incidence diffraction studies of thin films.

A multiple-imaging-plate detector system and focusing monochromator have been developed and successfully applied to the time-resolved study of phase transitions in Langmuir-Blodgett films by grazing-incidence X-ray diffraction (GIXD). The monochromator described here combines fixed-exit-beam height with sagittal focusing of the second crystal. The design is similar to that of Matsushita et al.

Protein Crystal Diffraction Patterns Using a Capillary-Focused Synchrotron X-ray Beam.

A paraboloidally tapered glass monocapillary was used to focus an 8 keV monochromated synchrotron bending-magnet X-ray beam into a 40 (+/-5) mum focal spot located 45 (+/-5) mm from the exit of the capillary. This focal spot had a measured intensity gain of 120 (+/-10) times the intensity present in an equivalent cross section of the unfocused beam from the monochromator. This focused beam was used to obtain oscillation diffraction patterns on image plates from a hen egg-white lysozyme protein crystal in two distinct geometries: one with the specimen crystal at the capillary exit and the other with the crystal at the beam focus.